To determine: The overall ∆G value when it is coupled to ATP hydrolysis
The reaction is
Introduction: The full form of ATP is adenosine triphosphate, which acts as both a precursor for RNA and is known as the energy currency of the cell. The ATP is known as energy currency because the hydrolysis of ATP generates energy and power most of the endergonic reactions.
Explanation of Solution
A molecule of ATP is made up of small components such as 5-carbon sugar, ribose, which act as a framework that attaches the other subunits; another component is adenine, and triphosphate is the third component which represents a chain of three phosphates. A
The ∆G of the product (glutamine) is 3.4 kcal/mol, while the free energy released during hydrolysis of ATP is
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Chapter 6 Solutions
BIOLOGY
- a) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) abovearrow_forwardThe standard free energy variation of the ATP hydrolysis reaction is ΔGº’ = -30.5 kJ / mol ATP + H2O ⇄ ADP + Pi In red blood cells, when the concentration of Pi is 1.6 mM, the real change in energy free is ΔG = - 50'2 kJ / mol. a) Calculate under these conditions what is the ratio [ATP] / [ADP] in the red blood cells. b) Determine the equilibrium constant K 'of the reaction outlined above. c) If the ADP concentration were 0.2mM, what would be the effective concentration of ATP corresponding to equilibrium.arrow_forwardConsider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·molarrow_forward
- From data in Table 13-6, calculate the ΔG′° value for the following reactions:(a) Phosphocreatine + ADP → creatine + ATP(b) ATP + fructose → ADP + fructose 6-phosphatearrow_forwardThe formation of glutamine from glutamate and ammonium ions requires 14.2 kJ mol-1 of energy input. It is driven by the hydrolysis of ATP to ADP mediated by the enzyme glutamine synthetase. {a) Given that the change in Gibbs energy for the hydrolysis of ATP corresponds to ΔG = -31 kJ mol-1, under the conditions prevailing in a typical cell , can the hydrolysis drive the formation of glutamine? (b) What amount {in moles) of ATP must be hydrolysed to form 1 mol glutamine? (c) Suppose that the radius of a typical cell is 10 μm and that inside it 106 ATP molecules are hydrolysed each second. What is the power density of the cell in watts per cubic metre (1W = 1 Js- 1)? (d) A computer battery delivers about 15 Wand has a volume of 100 cm3 Which has the greater power density, the biological cell or the battery?arrow_forwardIf the Go for ATP hydrolysis into ADP + inorganic phosphate is 7.3 kcal/mole, and the Go for glutamine synthesis from glutamic acid and NH3 is +3.4 kcal/mole, calculate the average Go for coupling these two reactions (glutamic acid + NH3 + ATP glutamine + ADP + inorganic phosphatearrow_forward
- ΔG°′ for the aldolase reaction is 22.8 kJ · mol−1. In the cell at 37°C, [DHAP]/ [GAP] = 5.5. Calculate the equilibrium ratio of [FBP]/[GAP] when [GAP] = 10−4 M.arrow_forwardA direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of ΔG′° can be calculated indirectly, however, from theequilibrium constants of two other enzymatic reactions having less favorable equilibrium constants:Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP.arrow_forwardFor part (b) of this problem, use the following standard reduction potentials, free energies, and nonequilibrium concentrations of reactants and products: Consider the last two steps in the alcoholic fermentation of glucose by brewer’s yeast: pyruvate + NADH + 2H+ → ethanol + NAD+ + CO2 (a) Do you predict that ∆S° for this reaction is > 0 or < 0? (b) Calculate the nonequilibrium concentration of ethanol in yeast cells, if ∆G = -38.3 kJ/mol for this reaction at pH = 7.4 and 37 °C when the reactants and products are at the concentrations given above. (c) How would a drop in pH affect ∆G for the reaction described in part (b)? (d) How would an increase in intracellular CO2 levels affect ∆G for the reaction in part (b)? (e) How would an increase in intracellular CO2 levels affect ∆G°′ for the reaction in part (b)?arrow_forward
- Given the following coupled reactions: phosphoenolpyruvate + H2O → pyruvate + Pi ΔG°'= -61.9 kJ/mol ATP + H2O → ADP + Pi ΔG°'= -30.5 kJ/mol write the overall reaction, calculate the ΔG°’, and determine if the reaction is exergonic or endergonic. The overall reaction is ______ + _______ → _______ + _________ The overall ΔG°’ is ________ kJ/mol. Therefore, the reaction is _______(exergonic/endergonic)arrow_forwardAG" = -69.5 kJ · mol- The percent efficiency of oxidative phosphorylation is 35%. Calculate the number of ATP generated by Complex I. Use 1 significant figure. The amount of ATP generated by Complex I is mol ATP. The equation for the overall reaction that occurs in Complex I is shown as: NADH + H+ + Q = NAD+ + QH2 Please explain! Thank you so much..arrow_forwardIntramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP. a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol) The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )arrow_forward
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